Two Forms of α-Glucosidase from Rice Seeds at the Milky Stage

Yamasaki, Yudai; Suzuki, Yukio

doi:10.1080/00021369.1980.10864024

Cited by 2 publications

(3 citation statements)

References 6 publications

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“…It was shown that the DNAs amplified by PCR, using primers designed for debranching enzymes (DBE), revealed marked differences between japonica and indica subspecies of rice (Nakamura et al, 2004). α-Glucosidase has been purified from various rice cultivars (Oryza sativa L.), namely Nipponbare (Nakai et al, 2007), Koshihikari (Awazuhara et al, 2000), Onnemochi (Ito et al, 1989), Shinsestsu (Takahashi et al, 1971), and Yashiromochi (Yamasaki and Suzuki, 1997), and from the germinating seeds of Thai rice (Eksittikul et al, 1993). The action of α-glucosidase may affect the accumulation of glucose during rice cooking (Mahashi et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Presence and Activity of Various Amylases in Rice: Effect on Texture and Leached Sugar Composition during Cooking

Tsujii¹,

Nagafuku

Miyake

et al. 2013

FSTR

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Amylase isozymes from non-glutinous japonica and indica rice types showed various band patterns, strengths and intensities based on zymography. Major bands were presumed to be α-and β-amylase according to their molecular weights; other amylases, 270 and 200 kDa in size, were also detected. Three debranching enzymes (DBEs) were detected from the dye pattern as well. Amylase activities were observed at pH 7.0 during rice cooking. However, the α-amylase activity at pH 7.0 was 50% lower than that at pH 5.0; DBE, β-amylase, and α-glucosidase values were similarly reduced by 25%, 90% and 99%, respectively. α-Amylase activity and DBE activities correlated positively with both the amount of maltooligomer leached during rice cooking and the adhesiveness of cooked rice. Thus, it is considered that the activity of amylase isozymes affects the palatability of cooked rice. Therefore, enzymes from rice endosperm may represent a new and highly useful biomarker for evaluating the palatability of cooked rice.

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Section: Introductionmentioning

confidence: 99%

Presence and Activity of Various Amylases in Rice: Effect on Texture and Leached Sugar Composition during Cooking

Tsujii¹,

Nagafuku

Miyake

et al. 2013

FSTR

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“…Rice species have been found to have multiple forms of α-glucosidases [32][33][34][35][36]. For example, α-glucosidases in dry seeds of Shinsetsu could be separated into two components by CM-Sepharose CL-6B chromatography at pH 8.3, a non-adsorbed component (Shinsetsu α-glucosidase I; OSG1) and an adsorbed component (Shinsetsu α-glucosidase II; OSG2) [34].…”

Section: Discussionmentioning

confidence: 99%

“…Rice α-glucosidase has been purified from dry seeds (i.e. after harvest) of various species, including Oryza sativa L., var Koshihikari [32], var Onnemochi [33], and var Shinsestu [34], from the ripening seeds of var Yashiromochi [35], and from the germinating seeds of Thai rice, Indica type [36]. All of these seeds contained multiple forms of α-glucosidases, which differed in molecular weight, isoelectric point, and kinetic parameters.…”

Section: Introductionmentioning

confidence: 99%

Multiple forms of α-glucosidase in rice seeds (Oryza sativa L., var Nipponbare)

et al. 2007

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Two isoforms of alpha-glucosidases (ONG2-I and ONG2-II) were purified from dry rice seeds (Oryza sativa L., var Nipponbare). Both ONG2-I and ONG2-II were the gene products of ONG2 mRNA expressed in ripening seeds. Each enzyme consisted of two components of 6kDa-peptide and 88kDa-peptide encoded by this order in ONG2 cDNA (ong2), and generated by post-translational proteolysis. The 88kDa-peptide of ONG2-II had 10 additional N-terminal amino acids compared with the 88kDa-peptide of ONG2-I. The peptides between 6kDa and 88kDa components (26 amino acids for ONG2-I and 16 for ONG2-II) were removed by post-translational proteolysis. Proteolysis induced changes in adsorption and degradation of insoluble starch granules. We also obtained three alpha-glucosidase cDNAs (ong1, ong3, and ong4) from ripening seeds. The ONG1, ONG2, and ONG4 genes were situated in distinct locus of rice genome. The transcripts encoding ONG2 and ONG3 were generated by alternative splicing. Members of alpha-glucosidase multigene family are differentially expressed during ripening and germinating stages in rice.

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Two Forms of α-Glucosidase from Rice Seeds at the Milky Stage

Cited by 2 publications

References 6 publications

Presence and Activity of Various Amylases in Rice: Effect on Texture and Leached Sugar Composition during Cooking

Presence and Activity of Various Amylases in Rice: Effect on Texture and Leached Sugar Composition during Cooking

Multiple forms of α-glucosidase in rice seeds (Oryza sativa L., var Nipponbare)

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